Tight-binding streptavidin ligands from a cyclic peptide library

Bioorganic and Medicinal Chemistry Letters

Volumn 8, Issue 17, 1998, Pages 2327-2332

  Zang, Xu ^a   Yu, Zhiguang ^a   Chu, Yen Ho ^a  

^a OHIO STATE UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ALKALINE PHOSPHATASE; AMINO ACID; CYCLOPEPTIDE; DISULFIDE; LACTAM; LIGAND; PEPTIDE LIBRARY; STREPTAVIDIN;

ARTICLE; BINDING AFFINITY; CYCLIZATION; ENZYME LINKED IMMUNOSORBENT ASSAY; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; LIGAND BINDING;

AMINO ACID SEQUENCE; INDICATORS AND REAGENTS; KINETICS; LIGANDS; MOLECULAR STRUCTURE; PEPTIDE LIBRARY; PEPTIDES, CYCLIC; STREPTAVIDIN; STRUCTURE-ACTIVITY RELATIONSHIP;

EID: 0032497399     PISSN: 0960894X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0960-894X(98)00421-1     Document Type: Article

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44. 44. Ac-HPQFG-TentaGel was identified as a ligand to streptavidin from a linear peptide library prepared in our library (Yu, Z.; Chu, Y.-H. unpublished results).
45. 4, 137 mM NaCl, 2.7 mM KCl, and 0.1% Tween-20, pH 7.2) twice and 2x TBS buffer (2.5 mM Tris, 13.7 mM NaCl, 0.27 mM KCl, pH 8.0) once. The soluble substrate p-nitrophenyl phosphate (pNPP) was added (0.25 mL/well) and color development was allowed to develop for 30 min. The reaction of pNPP hydrolysis was terminated with 3 N NaOH (0.25mL) and the solution was diluted to 1.0 mL with water. Absorbance was recorded at 405 nm.
46. 2 were chosen from each deconvolution step where the specific amino acid gave low inhibition at that position.
47. 47. Both library-identified cyclic peptide ligands 1 and 2 were used to incubate with a streptavidin-immobilized affinity column (Pierce Chemical Co.) for 30 min. After the affinity column was washed with the binding buffer (10 columns volume), a solution containing biotin (1 mM, 5 columns volume) was used to elute out the bound cyclic peptide. All eluting fractions were collected and analyzed by MALDI MS (Kratos Kompact MALDI-III). The cyclic peptide ligands were detected in the eluted fractions after the biotin-washing step, but not in the fractions after binding buffer washing step (Zang, X.; Chu, Y.-H. unpublished result).
48. 50 Values. Using the same ELISA method described in ref 45, peptide was added to the blocking buffer containing 1:2,500 diluted SAP conjugate. This peptide-SAP mixture was then systematically diluted using a solution containing SAP conjugate (1:2,500 dilution) to prepare solutions of peptide with concentrations ranging from 10 nM to 1mM, while keeping the SAP conjugate concentration constant. At each peptide concentration, the peptide-SAP conjugate mixture was incubated for 12 h and then mixed with the straptavidin-binding Ac-HPQFG on TentaGel resin for 30 min. After removing the peptide-SAP solution and washing the resin with 1x PBST twice and 2x TBS once, the soluble substrate pNPP was added (0.25 mL/well) and color development was allowed to proceed for 30 min. The hydrolysis of pNPP was stopped using 3 N NaOH and subsequently diluted to a final volume of 1.0 mL with water. Absorbance were recorded at 405 nm.